Bradykinin-induced phosphoinositide-dependent responses in protein kinase C down-regulated NCB-20 cells

Yukio Okano; Haruhiro Higashida; Fu Tao; Takayuki Sakai; Yoshinori Nozawa

doi:10.1016/0197-0186(91)90175-D

Bradykinin-induced phosphoinositide-dependent responses in protein kinase C down-regulated NCB-20 cells

Yukio Okano, Haruhiro Higashida, Fu Tao, Takayuki Sakai, Yoshinori Nozawa^*

^*Corresponding author for this work

Pathology

Research output: Contribution to journal › Article › peer-review

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Abstract

Long-term (12 h) incubation of NCB-20 neuroblastoma × Chinese hamster brain cell hybrid cells with phorbol dibutylate caused a decrease in the enzyme activity of protein kinase C (PKC). Under these conditions, the formation of inositol 1,4,5-trisphosphate [Ins(1,4,5)P₃] and the mobilization of intracellular Ca²⁺ triggered by bradykinin (BK), were significantly increased. The alterations in BK-triggered membrane currents in the PKC down-regulated cells were also observed: enhancement of outward currents and decreased inward currents. These results strongly suggested that down-regulation of PKC enhanced BK-induced phosphoinositide metabolism by relieving from the negative feedback control operating between the receptor and phospholipase C, and that the increased Ca²⁺ responses due to accumulated Ins(1,4,5)P₃ lead to enhanced outward currents.

Original language	English (US)
Pages (from-to)	419-424
Number of pages	6
Journal	Neurochemistry International
Volume	18
Issue number	3
DOIs	https://doi.org/10.1016/0197-0186(91)90175-D
State	Published - 1991

ASJC Scopus subject areas

Cellular and Molecular Neuroscience
Cell Biology

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10.1016/0197-0186(91)90175-D

Cite this

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title = "Bradykinin-induced phosphoinositide-dependent responses in protein kinase C down-regulated NCB-20 cells",

abstract = "Long-term (12 h) incubation of NCB-20 neuroblastoma × Chinese hamster brain cell hybrid cells with phorbol dibutylate caused a decrease in the enzyme activity of protein kinase C (PKC). Under these conditions, the formation of inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] and the mobilization of intracellular Ca2+ triggered by bradykinin (BK), were significantly increased. The alterations in BK-triggered membrane currents in the PKC down-regulated cells were also observed: enhancement of outward currents and decreased inward currents. These results strongly suggested that down-regulation of PKC enhanced BK-induced phosphoinositide metabolism by relieving from the negative feedback control operating between the receptor and phospholipase C, and that the increased Ca2+ responses due to accumulated Ins(1,4,5)P3 lead to enhanced outward currents.",

author = "Yukio Okano and Haruhiro Higashida and Fu Tao and Takayuki Sakai and Yoshinori Nozawa",

year = "1991",

doi = "10.1016/0197-0186(91)90175-D",

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T1 - Bradykinin-induced phosphoinositide-dependent responses in protein kinase C down-regulated NCB-20 cells

AU - Okano, Yukio

AU - Higashida, Haruhiro

AU - Tao, Fu

AU - Sakai, Takayuki

AU - Nozawa, Yoshinori

PY - 1991

Y1 - 1991

N2 - Long-term (12 h) incubation of NCB-20 neuroblastoma × Chinese hamster brain cell hybrid cells with phorbol dibutylate caused a decrease in the enzyme activity of protein kinase C (PKC). Under these conditions, the formation of inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] and the mobilization of intracellular Ca2+ triggered by bradykinin (BK), were significantly increased. The alterations in BK-triggered membrane currents in the PKC down-regulated cells were also observed: enhancement of outward currents and decreased inward currents. These results strongly suggested that down-regulation of PKC enhanced BK-induced phosphoinositide metabolism by relieving from the negative feedback control operating between the receptor and phospholipase C, and that the increased Ca2+ responses due to accumulated Ins(1,4,5)P3 lead to enhanced outward currents.

AB - Long-term (12 h) incubation of NCB-20 neuroblastoma × Chinese hamster brain cell hybrid cells with phorbol dibutylate caused a decrease in the enzyme activity of protein kinase C (PKC). Under these conditions, the formation of inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] and the mobilization of intracellular Ca2+ triggered by bradykinin (BK), were significantly increased. The alterations in BK-triggered membrane currents in the PKC down-regulated cells were also observed: enhancement of outward currents and decreased inward currents. These results strongly suggested that down-regulation of PKC enhanced BK-induced phosphoinositide metabolism by relieving from the negative feedback control operating between the receptor and phospholipase C, and that the increased Ca2+ responses due to accumulated Ins(1,4,5)P3 lead to enhanced outward currents.

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Bradykinin-induced phosphoinositide-dependent responses in protein kinase C down-regulated NCB-20 cells

Abstract

ASJC Scopus subject areas

UN SDGs

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